PRMT2

Protein arginine methyltransferase 2

PDB rendering based on 1x2p.

Available structures
PDB	1x2p

Identifiers

Symbols

PRMT2; HRMT1L1; MGC111373

External IDs

OMIM: 601961 MGI: 1316652 HomoloGene: 55587 GeneCards: PRMT2 Gene

EC number

2.1.1.125

Gene Ontology
Molecular function	• transcription coactivator activity • signal transducer activity • protein binding • methyltransferase activity • histone-arginine N-methyltransferase activity • protein-arginine N-methyltransferase activity • transferase activity • estrogen receptor binding • estrogen receptor binding • progesterone receptor binding • identical protein binding • protein homodimerization activity • retinoic acid receptor binding • peroxisome proliferator activated receptor binding • thyroid hormone receptor binding • androgen receptor binding
Cellular component	• nucleus • cytoplasm • cytosol • Rb-E2F complex
Biological process	• protein methylation • induction of apoptosis • signal transduction • negative regulation of NF-kappaB transcription factor activity • peptidyl-arginine N-methylation • negative regulation of transcription, DNA-dependent • positive regulation of transcription, DNA-dependent • developmental cell growth • regulation of androgen receptor signaling pathway • negative regulation of G1/S transition of mitotic cell cycle
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 21:
48.06 – 48.09 Mb

Chr 10:
75.67 – 75.7 Mb

PubMed search

[1]

[2]

Protein arginine N-methyltransferase 2 is an enzyme that in humans is encoded by the PRMT2 gene.^[1]^[2]

Interactions

PRMT2 has been shown to interact with Estrogen receptor alpha^[3] and HNRPUL1.^[4]

References

^ Scott HS, Antonarakis SE, Lalioti MD, Rossier C, Silver PA, Henry MF (Jun 1998). "Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)". Genomics 48 (3): 330–40. doi:10.1006/geno.1997.5190. PMID 9545638.
^ "Entrez Gene: PRMT2 protein arginine methyltransferase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3275.
^ Qi, Chao; Chang Jeffrey, Zhu Yiwei, Yeldandi Anjana V, Rao Sambasiva M, Zhu Yi-Jun (Aug. 2002). "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha". J. Biol. Chem. (United States) 277 (32): 28624–30. doi:10.1074/jbc.M201053200. ISSN 0021-9258. PMID 12039952.
^ Kzhyshkowska, J; Schütt H, Liss M, Kremmer E, Stauber R, Wolf H, Dobner T (Sep. 2001). "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1". Biochem. J. (England) 358 (Pt 2): 305–14. doi:10.1042/0264-6021:3580305. ISSN 0264-6021. PMC 1222062. PMID 11513728. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222062.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Andersson B, Wentland MA, Ricafrente JY et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146.
Katsanis N, Yaspo ML, Fisher EM (1997). "Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene". Mamm. Genome 8 (7): 526–9. doi:10.1007/s003359900491. PMID 9196002.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Hattori M, Fujiyama A, Taylor TD et al. (2000). "The DNA sequence of human chromosome 21". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
Kzhyshkowska J, Schütt H, Liss M et al. (2001). "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1". Biochem. J. 358 (Pt 2): 305–14. doi:10.1042/0264-6021:3580305. PMC 1222062. PMID 11513728. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222062.
Qi C, Chang J, Zhu Y et al. (2002). "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha". J. Biol. Chem. 277 (32): 28624–30. doi:10.1074/jbc.M201053200. PMID 12039952.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Lehner B, Semple JI, Brown SE et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Rual JF, Venkatesan K, Hao T et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Ganesh L, Yoshimoto T, Moorthy NC et al. (2006). "Protein Methyltransferase 2 Inhibits NF-κB Function and Promotes Apoptosis". Mol. Cell. Biol. 26 (10): 3864–74. doi:10.1128/MCB.26.10.3864-3874.2006. PMC 1488990. PMID 16648481. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1488990.

PDB gallery

1x2p: Solution structure of the SH3 domain of the Protein arginine N-methyltransferase 2

PRMT2

Interactions

References

Further reading